Final Activity Report Summary - DPP6 AND 10 PARTNERS (Investigate for cellular partners of DPP6 and DPP10 through novel technologies)
Potassium channels contribute to many cellular processes, including the control of cell volume, membrane potential, neuronal excitability, muscle contractility and the secretion of salts, hormones and neurotransmitters. Their activities can be regulated by a number of accessory proteins. We and other research groups reported that two members of an ecto-peptidase family, DPP6 and DPP10, whose function was previously unknown, may interact with some voltage-gated potassium channels of the KCND gene family and modulates their function, through a mechanism still unknown.
Our research is focussed on the elucidation of the physiological role of DPP6 and DPP10 through the identification of their binding partners and characterisation of their structure-function relationships. We are currently using an innovative and interdisciplinary approach, based on novel HTS (high throughput screening) selection of interaction partners, including recombinant antibodies targeting the different functional domains of DPP6 and DPP10. Our approaches includes the phage display, protein complementation assay and yeast two-hybrid technologies and led to the identification of some proteins of the cytoskeleton as putative binding partners of DPP10 and the development of three isoform-specific recombinant antibodies targeting the intracellular domain of DPP6.
These data will add impetus to the development of inhibitor molecules for pharmacological or therapeutic use.
Our research is focussed on the elucidation of the physiological role of DPP6 and DPP10 through the identification of their binding partners and characterisation of their structure-function relationships. We are currently using an innovative and interdisciplinary approach, based on novel HTS (high throughput screening) selection of interaction partners, including recombinant antibodies targeting the different functional domains of DPP6 and DPP10. Our approaches includes the phage display, protein complementation assay and yeast two-hybrid technologies and led to the identification of some proteins of the cytoskeleton as putative binding partners of DPP10 and the development of three isoform-specific recombinant antibodies targeting the intracellular domain of DPP6.
These data will add impetus to the development of inhibitor molecules for pharmacological or therapeutic use.